Grafting the ALFA Tag for Structural Studies of Aquaporin Z

Authors

Lauren Stover
Hanieh Bahramimoghaddam
Lie Wang
Samantha Schrecke
Gaya P Yadav
Ming Zhou
Arthur Laganowsky

Language

English

Publication Date

6-1-2024

Journal

Journal of Structural Biology: X

DOI

10.1016/j.yjsbx.2024.100097

PMID

38361954

PMCID

PMC10867769

PubMedCentral® Posted Date

2-2-2024

PubMedCentral® Full Text Version

Post-print

Abstract

Aquaporin Z (AqpZ), a bacterial water channel, forms a tetrameric complex and, like many other membrane proteins, activity is regulated by lipids. Various methods have been developed to facilitate structure determination of membrane proteins, such as the use of antibodies. Here, we graft onto AqpZ the ALFA tag (AqpZ-ALFA), an alpha helical epitope, to make use of the high-affinity anti-ALFA nanobody (nB). Native mass spectrometry reveals the AqpZ-ALFA fusion forms a stable, 1:1 complex with nB. Single-particle cryogenic electron microscopy studies reveal the octameric (AqpZ-ALFA)

Published Open-Access

yes

Recommended Citation

Stover, Lauren; Bahramimoghaddam, Hanieh; Wang, Lie; et al., "Grafting the ALFA Tag for Structural Studies of Aquaporin Z" (2024). Faculty, Staff and Students Publications. 6268.
https://digitalcommons.library.tmc.edu/baylor_docs/6268